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In vivo phosphorylation of isocitrate lyase from Escherichia coli D5H3G7.

This report describes the in vivo phosphorylation of isocitrate lyase and examines the possible consequences to the control of the Kreb's cycle and glyoxylate bypass. NADP-specific isocitrate dehydrogenase from E. coli was the first bacterial protein whose enzymic activity was shown to be modulated by reversible phosphorylation. This enzyme has been thought to be solely responsible for the partitioning of isocitrate between the Kreb's cycle and glyoxylate bypass. No studies to date have examined the possible role of isocitrate lyase in controlling this flux.[1]

References

  1. In vivo phosphorylation of isocitrate lyase from Escherichia coli D5H3G7. Hoyt, J.C., Reeves, H.C. Biochem. Biophys. Res. Commun. (1988) [Pubmed]
 
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